Full text data of TNPO3
TNPO3
(IPO12)
[Confidence: low (only semi-automatic identification from reviews)]
Transportin-3 (Importin-12; Imp12; Transportin-SR; TRN-SR)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Transportin-3 (Importin-12; Imp12; Transportin-SR; TRN-SR)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y5L0
ID TNPO3_HUMAN Reviewed; 923 AA.
AC Q9Y5L0; A4D1K9; C9IZM0; Q6NUM1; Q96G71; Q96GU9; Q9Y3R2;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-JAN-2008, sequence version 3.
DT 22-JAN-2014, entry version 102.
DE RecName: Full=Transportin-3;
DE AltName: Full=Importin-12;
DE Short=Imp12;
DE AltName: Full=Transportin-SR;
DE Short=TRN-SR;
GN Name=TNPO3; Synonyms=IPO12;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
RP SFRS1 AND SFRS2.
RX PubMed=10366588; DOI=10.1083/jcb.145.6.1145;
RA Kataoka N., Bachorik J.L., Dreyfuss G.;
RT "Transportin-SR, a nuclear import receptor for SR proteins.";
RL J. Cell Biol. 145:1145-1152(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Kutay U., Izaurralde E., Hartmann E., Goerlich D.;
RT "A human homologue of yeast Mtr10p and its role in nuclear protein
RT import.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Colon;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA Mural R.J., Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 586-923 (ISOFORM 3).
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, INTERACTION WITH SFRS1, AND SUBCELLULAR LOCATION.
RX PubMed=10713112; DOI=10.1074/jbc.275.11.7950;
RA Lai M.-C., Lin R.-I., Huang S.-Y., Tsai C.-W., Tarn W.-Y.;
RT "A human importin-beta family protein, transportin-SR2, interacts with
RT the phosphorylated RS domain of SR proteins.";
RL J. Biol. Chem. 275:7950-7957(2000).
RN [8]
RP FUNCTION, AND INTERACTION WITH SFRS1 AND NUP62.
RX PubMed=11517331; DOI=10.1073/pnas.181354098;
RA Lai M.-C., Lin R.-I., Tarn W.-Y.;
RT "Transportin-SR2 mediates nuclear import of phosphorylated SR
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:10154-10159(2001).
RN [9]
RP FUNCTION, AND INTERACTION WITH RBM4.
RX PubMed=12628928; DOI=10.1093/emboj/cdg126;
RA Lai M.-C., Kuo H.-W., Chang W.-C., Tarn W.-Y.;
RT "A novel splicing regulator shares a nuclear import pathway with SR
RT proteins.";
RL EMBO J. 22:1359-1369(2003).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-896, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Seems to function in nuclear protein import as nuclear
CC transport receptor. In vitro, mediates the nuclear import of
CC splicing factor SR proteins RBM4, SFRS1 and SFRS2, by recognizing
CC phosphorylated RS domains.
CC -!- SUBUNIT: Interacts with phosphorylated SFRS1 and SFRS2. Interacts
CC with NUP62 and RBM4.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=2; Synonyms=TRN-SR2;
CC IsoId=Q9Y5L0-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9Y5L0-1; Sequence=VSP_030174;
CC Name=3;
CC IsoId=Q9Y5L0-3; Sequence=VSP_011178;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q9Y5L0-5; Sequence=VSP_045494;
CC Note=No experimental confirmation available;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD38537.1; Type=Frameshift; Positions=920;
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DR EMBL; AF145029; AAD38537.1; ALT_FRAME; mRNA.
DR EMBL; AJ133769; CAB42643.1; -; mRNA.
DR EMBL; AK225999; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC018639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236950; EAL24106.1; -; Genomic_DNA.
DR EMBL; BC009221; AAH09221.2; -; mRNA.
DR RefSeq; NP_001177957.2; NM_001191028.2.
DR RefSeq; NP_036602.1; NM_012470.3.
DR UniGene; Hs.193613; -.
DR ProteinModelPortal; Q9Y5L0; -.
DR SMR; Q9Y5L0; 7-923.
DR IntAct; Q9Y5L0; 6.
DR MINT; MINT-1194798; -.
DR STRING; 9606.ENSP00000265388; -.
DR PhosphoSite; Q9Y5L0; -.
DR DMDM; 166215035; -.
DR PaxDb; Q9Y5L0; -.
DR PRIDE; Q9Y5L0; -.
DR DNASU; 23534; -.
DR Ensembl; ENST00000265388; ENSP00000265388; ENSG00000064419.
DR Ensembl; ENST00000471234; ENSP00000418646; ENSG00000064419.
DR GeneID; 23534; -.
DR KEGG; hsa:23534; -.
DR UCSC; uc010llz.2; human.
DR CTD; 23534; -.
DR GeneCards; GC07M128594; -.
DR HGNC; HGNC:17103; TNPO3.
DR HPA; HPA039555; -.
DR MIM; 610032; gene.
DR neXtProt; NX_Q9Y5L0; -.
DR Orphanet; 55595; Autosomal dominant limb-girdle muscular dystrophy type 1F.
DR Orphanet; 186; Primary biliary cirrhosis.
DR PharmGKB; PA134888159; -.
DR eggNOG; NOG237172; -.
DR HOGENOM; HOG000273876; -.
DR HOVERGEN; HBG057505; -.
DR KO; K15436; -.
DR OrthoDB; EOG718KC9; -.
DR GeneWiki; Transportin-3; -.
DR GenomeRNAi; 23534; -.
DR NextBio; 46030; -.
DR PRO; PR:Q9Y5L0; -.
DR ArrayExpress; Q9Y5L0; -.
DR Bgee; Q9Y5L0; -.
DR CleanEx; HS_TNPO3; -.
DR Genevestigator; Q9Y5L0; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0004872; F:receptor activity; TAS:ProtInc.
DR GO; GO:0035048; P:splicing factor protein import into nucleus; IDA:UniProtKB.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013598; Exportin-1/Importin-b-like.
DR Pfam; PF08389; Xpo1; 1.
DR SUPFAM; SSF48371; SSF48371; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Nucleus; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1 923 Transportin-3.
FT /FTId=PRO_0000120781.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 896 896 Phosphothreonine.
FT VAR_SEQ 453 453 P -> PKKPFSNAACHHSLLFGQNITSEISNCEYLPPVLR
FT (in isoform 1).
FT /FTId=VSP_030174.
FT VAR_SEQ 500 563 Missing (in isoform 4).
FT /FTId=VSP_045494.
FT VAR_SEQ 904 923 SAEECKQVCWALRDFTRLFR -> RNVFFN (in
FT isoform 3).
FT /FTId=VSP_011178.
FT CONFLICT 87 87 R -> W (in Ref. 1; AAD38537).
FT CONFLICT 265 265 L -> S (in Ref. 3; AK225999).
FT CONFLICT 358 358 D -> G (in Ref. 3; AK225999).
FT CONFLICT 480 480 T -> A (in Ref. 3; AK225999).
FT CONFLICT 624 624 P -> L (in Ref. 3; AK225999).
SQ SEQUENCE 923 AA; 104203 MW; CF7CDC14CDBA56AB CRC64;
MEGAKPTLQL VYQAVQALYH DPDPSGKERA SFWLGELQRS VHAWEISDQL LQIRQDVESC
YFAAQTMKMK IQTSFYELPT DSHASLRDSL LTHIQNLKDL SPVIVTQLAL AIADLALQMP
SWKGCVQTLV EKYSNDVTSL PFLLEILTVL PEEVHSRSLR IGANRRTEII EDLAFYSSTV
VSLLMTCVEK AGTDEKMLMK VFRCLGSWFN LGVLDSNFMA NNKLLALLFE VLQQDKTSSN
LHEAASDCVC SALYAIENVE TNLPLAMQLF QGVLTLETAY HMAVAREDLD KVLNYCRIFT
ELCETFLEKI VCTPGQGLGD LRTLELLLIC AGHPQYEVVE ISFNFWYRLG EHLYKTNDEV
IHGIFKAYIQ RLLHALARHC QLEPDHEGVP EETDDFGEFR MRVSDLVKDL IFLIGSMECF
AQLYSTLKEG NPPWEVTEAV LFIMAAIAKS VDPENNPTLV EVLEGVVRLP ETVHTAVRYT
SIELVGEMSE VVDRNPQFLD PVLGYLMKGL CEKPLASAAA KAIHNICSVC RDHMAQHFNG
LLEIARSLDS FLLSPEAAVG LLKGTALVLA RLPLDKITEC LSELCSVQVM ALKKLLSQEP
SNGISSDPTV FLDRLAVIFR HTNPIVENGQ THPCQKVIQE IWPVLSETLN KHRADNRIVE
RCCRCLRFAV RCVGKGSAAL LQPLVTQMVN VYHVHQHSCF LYLGSILVDE YGMEEGCRQG
LLDMLQALCI PTFQLLEQQN GLQNHPDTVD DLFRLATRFI QRSPVTLLRS QVVIPILQWA
IASTTLDHRD ANCSVMRFLR DLIHTGVAND HEEDFELRKE LIGQVMNQLG QQLVSQLLHT
CCFCLPPYTL PDVAEVLWEI MQVDRPTFCR WLENSLKGLP KETTVGAVTV THKQLTDFHK
QVTSAEECKQ VCWALRDFTR LFR
//
ID TNPO3_HUMAN Reviewed; 923 AA.
AC Q9Y5L0; A4D1K9; C9IZM0; Q6NUM1; Q96G71; Q96GU9; Q9Y3R2;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-JAN-2008, sequence version 3.
DT 22-JAN-2014, entry version 102.
DE RecName: Full=Transportin-3;
DE AltName: Full=Importin-12;
DE Short=Imp12;
DE AltName: Full=Transportin-SR;
DE Short=TRN-SR;
GN Name=TNPO3; Synonyms=IPO12;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
RP SFRS1 AND SFRS2.
RX PubMed=10366588; DOI=10.1083/jcb.145.6.1145;
RA Kataoka N., Bachorik J.L., Dreyfuss G.;
RT "Transportin-SR, a nuclear import receptor for SR proteins.";
RL J. Cell Biol. 145:1145-1152(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Kutay U., Izaurralde E., Hartmann E., Goerlich D.;
RT "A human homologue of yeast Mtr10p and its role in nuclear protein
RT import.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Colon;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA Mural R.J., Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 586-923 (ISOFORM 3).
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, INTERACTION WITH SFRS1, AND SUBCELLULAR LOCATION.
RX PubMed=10713112; DOI=10.1074/jbc.275.11.7950;
RA Lai M.-C., Lin R.-I., Huang S.-Y., Tsai C.-W., Tarn W.-Y.;
RT "A human importin-beta family protein, transportin-SR2, interacts with
RT the phosphorylated RS domain of SR proteins.";
RL J. Biol. Chem. 275:7950-7957(2000).
RN [8]
RP FUNCTION, AND INTERACTION WITH SFRS1 AND NUP62.
RX PubMed=11517331; DOI=10.1073/pnas.181354098;
RA Lai M.-C., Lin R.-I., Tarn W.-Y.;
RT "Transportin-SR2 mediates nuclear import of phosphorylated SR
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:10154-10159(2001).
RN [9]
RP FUNCTION, AND INTERACTION WITH RBM4.
RX PubMed=12628928; DOI=10.1093/emboj/cdg126;
RA Lai M.-C., Kuo H.-W., Chang W.-C., Tarn W.-Y.;
RT "A novel splicing regulator shares a nuclear import pathway with SR
RT proteins.";
RL EMBO J. 22:1359-1369(2003).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-896, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Seems to function in nuclear protein import as nuclear
CC transport receptor. In vitro, mediates the nuclear import of
CC splicing factor SR proteins RBM4, SFRS1 and SFRS2, by recognizing
CC phosphorylated RS domains.
CC -!- SUBUNIT: Interacts with phosphorylated SFRS1 and SFRS2. Interacts
CC with NUP62 and RBM4.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=2; Synonyms=TRN-SR2;
CC IsoId=Q9Y5L0-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9Y5L0-1; Sequence=VSP_030174;
CC Name=3;
CC IsoId=Q9Y5L0-3; Sequence=VSP_011178;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q9Y5L0-5; Sequence=VSP_045494;
CC Note=No experimental confirmation available;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD38537.1; Type=Frameshift; Positions=920;
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DR EMBL; AF145029; AAD38537.1; ALT_FRAME; mRNA.
DR EMBL; AJ133769; CAB42643.1; -; mRNA.
DR EMBL; AK225999; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC018639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236950; EAL24106.1; -; Genomic_DNA.
DR EMBL; BC009221; AAH09221.2; -; mRNA.
DR RefSeq; NP_001177957.2; NM_001191028.2.
DR RefSeq; NP_036602.1; NM_012470.3.
DR UniGene; Hs.193613; -.
DR ProteinModelPortal; Q9Y5L0; -.
DR SMR; Q9Y5L0; 7-923.
DR IntAct; Q9Y5L0; 6.
DR MINT; MINT-1194798; -.
DR STRING; 9606.ENSP00000265388; -.
DR PhosphoSite; Q9Y5L0; -.
DR DMDM; 166215035; -.
DR PaxDb; Q9Y5L0; -.
DR PRIDE; Q9Y5L0; -.
DR DNASU; 23534; -.
DR Ensembl; ENST00000265388; ENSP00000265388; ENSG00000064419.
DR Ensembl; ENST00000471234; ENSP00000418646; ENSG00000064419.
DR GeneID; 23534; -.
DR KEGG; hsa:23534; -.
DR UCSC; uc010llz.2; human.
DR CTD; 23534; -.
DR GeneCards; GC07M128594; -.
DR HGNC; HGNC:17103; TNPO3.
DR HPA; HPA039555; -.
DR MIM; 610032; gene.
DR neXtProt; NX_Q9Y5L0; -.
DR Orphanet; 55595; Autosomal dominant limb-girdle muscular dystrophy type 1F.
DR Orphanet; 186; Primary biliary cirrhosis.
DR PharmGKB; PA134888159; -.
DR eggNOG; NOG237172; -.
DR HOGENOM; HOG000273876; -.
DR HOVERGEN; HBG057505; -.
DR KO; K15436; -.
DR OrthoDB; EOG718KC9; -.
DR GeneWiki; Transportin-3; -.
DR GenomeRNAi; 23534; -.
DR NextBio; 46030; -.
DR PRO; PR:Q9Y5L0; -.
DR ArrayExpress; Q9Y5L0; -.
DR Bgee; Q9Y5L0; -.
DR CleanEx; HS_TNPO3; -.
DR Genevestigator; Q9Y5L0; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0004872; F:receptor activity; TAS:ProtInc.
DR GO; GO:0035048; P:splicing factor protein import into nucleus; IDA:UniProtKB.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013598; Exportin-1/Importin-b-like.
DR Pfam; PF08389; Xpo1; 1.
DR SUPFAM; SSF48371; SSF48371; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Nucleus; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1 923 Transportin-3.
FT /FTId=PRO_0000120781.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 896 896 Phosphothreonine.
FT VAR_SEQ 453 453 P -> PKKPFSNAACHHSLLFGQNITSEISNCEYLPPVLR
FT (in isoform 1).
FT /FTId=VSP_030174.
FT VAR_SEQ 500 563 Missing (in isoform 4).
FT /FTId=VSP_045494.
FT VAR_SEQ 904 923 SAEECKQVCWALRDFTRLFR -> RNVFFN (in
FT isoform 3).
FT /FTId=VSP_011178.
FT CONFLICT 87 87 R -> W (in Ref. 1; AAD38537).
FT CONFLICT 265 265 L -> S (in Ref. 3; AK225999).
FT CONFLICT 358 358 D -> G (in Ref. 3; AK225999).
FT CONFLICT 480 480 T -> A (in Ref. 3; AK225999).
FT CONFLICT 624 624 P -> L (in Ref. 3; AK225999).
SQ SEQUENCE 923 AA; 104203 MW; CF7CDC14CDBA56AB CRC64;
MEGAKPTLQL VYQAVQALYH DPDPSGKERA SFWLGELQRS VHAWEISDQL LQIRQDVESC
YFAAQTMKMK IQTSFYELPT DSHASLRDSL LTHIQNLKDL SPVIVTQLAL AIADLALQMP
SWKGCVQTLV EKYSNDVTSL PFLLEILTVL PEEVHSRSLR IGANRRTEII EDLAFYSSTV
VSLLMTCVEK AGTDEKMLMK VFRCLGSWFN LGVLDSNFMA NNKLLALLFE VLQQDKTSSN
LHEAASDCVC SALYAIENVE TNLPLAMQLF QGVLTLETAY HMAVAREDLD KVLNYCRIFT
ELCETFLEKI VCTPGQGLGD LRTLELLLIC AGHPQYEVVE ISFNFWYRLG EHLYKTNDEV
IHGIFKAYIQ RLLHALARHC QLEPDHEGVP EETDDFGEFR MRVSDLVKDL IFLIGSMECF
AQLYSTLKEG NPPWEVTEAV LFIMAAIAKS VDPENNPTLV EVLEGVVRLP ETVHTAVRYT
SIELVGEMSE VVDRNPQFLD PVLGYLMKGL CEKPLASAAA KAIHNICSVC RDHMAQHFNG
LLEIARSLDS FLLSPEAAVG LLKGTALVLA RLPLDKITEC LSELCSVQVM ALKKLLSQEP
SNGISSDPTV FLDRLAVIFR HTNPIVENGQ THPCQKVIQE IWPVLSETLN KHRADNRIVE
RCCRCLRFAV RCVGKGSAAL LQPLVTQMVN VYHVHQHSCF LYLGSILVDE YGMEEGCRQG
LLDMLQALCI PTFQLLEQQN GLQNHPDTVD DLFRLATRFI QRSPVTLLRS QVVIPILQWA
IASTTLDHRD ANCSVMRFLR DLIHTGVAND HEEDFELRKE LIGQVMNQLG QQLVSQLLHT
CCFCLPPYTL PDVAEVLWEI MQVDRPTFCR WLENSLKGLP KETTVGAVTV THKQLTDFHK
QVTSAEECKQ VCWALRDFTR LFR
//
MIM
610032
*RECORD*
*FIELD* NO
610032
*FIELD* TI
*610032 TRANSPORTIN 3; TNPO3
;;TRANSPORTIN-SR; TRNSR
*FIELD* TX
DESCRIPTION
TNPO3 is a nuclear import receptor for serine/arginine-rich (SR)
read moreproteins, which are essential precursor-mRNA splicing factors (Kataoka
et al., 1999).
CLONING
Using the RS domain of ASF/SF2 (SFRS1; 600812) as bait in a yeast
2-hybrid screen, followed by screening a HeLa cell cDNA library, Kataoka
et al. (1999) cloned TNPO3, which they designated TRNSR. The deduced
975-amino acid protein has a calculated molecular mass of 109.8 kD. It
shows significant similarity to other importin-beta/transportin family
members (e.g., TNPO1; 602901), including a region required for RanGTP
(see RAN; 601179) binding.
By yeast 2-hybrid analysis using the RS domain of the E2 protein of
human papillomavirus (HPV)-5 as bait, Lai et al. (2000) cloned a TNPO3
splice variant, TRNSR2, from a HeLa cell cDNA library. The deduced
923-amino acid TRNSR2 protein lacks 2 regions of about 30 amino acids
each found in the TRNSR protein identified by Kataoka et al. (1999).
Northern blot analysis detected ubiquitous expression of a 4.5-kb
transcript, with highest expression in testis. Epitope-tagged TRNSR2
localized throughout transfected HeLa cells, but a mutant lacking the
N-terminal region colocalized with splicing factor SC35 (SFRS2; 600813)
in nuclear speckles.
GENE FUNCTION
Using in vitro binding assays, Kataoka et al. (1999) found that TRNSR
bound the RS domains of ASF/SF2 and SC35 directly, but it did not
interact with other protein domains examined. A Ran mutant mimicking
RanGTP, which promotes dissociation of import receptor-cargo complexes,
abolished binding of TRNSR to RS domains. In an in vitro import assay,
TRNSR efficiently imported the RS domains of ASF/SF2 and SC35 into the
nucleus in an ATP- and RanGDP-dependent manner. Far Western blot
analysis showed that TRNSR bound several proteins within an SR protein
fraction purified from HeLa nuclear extracts.
Using yeast 2-hybrid analysis, Lai et al. (2000) showed that TRNSR2
interacted with the RS domain in the hinge region of HPV-5 E2. The
C-terminal 400 amino acids of TRNSR2 also interacted with ASF/SF2, SC35,
and TRA2-beta (SFRS10; 602719). Mutation analysis confirmed that TRNSR2
interacted with the N-terminal RS domain of TRA2-beta, but not with the
RNA-binding domains of ASF and TRA2-beta. In vitro pull-down assays
revealed that only ASF containing phosphorylated RS domains interacted
with TRNSR2 in HeLa cell extracts. Lai et al. (2000) concluded that
TRNSR2 has a role in cellular trafficking of phosphorylated SR proteins.
Using a large-scale small interfering RNA screen to identify host
factors required by human immunodeficiency virus (HIV)-1 (see 609423),
Brass et al. (2008) identified more than 250 HIV-dependency factors
(HDFs), 79 of which showed significantly higher expression in immune
tissues compared with other tissues. Depletion of the HDF TNPO3, a
karyopherin, resulted in HIV inhibition after reverse transcription, but
before integration. Brass et al. (2008) proposed that targeting of HDFs
essential for the viral cycle but not critical for the host may avoid
drug resistance due to viral diversity and escape mutation.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the TNPO3
gene to chromosome 7 (TMAP D7S2931).
MOLECULAR GENETICS
- Association with Primary Biliary Cirrhosis
For a discussion of a possible association between variation in the
TNPO3 gene and primary biliary cirrhosis, see PBC4 (614220).
*FIELD* RF
1. Brass, A. L.; Dykxhoorn, D. M.; Benita, Y.; Yan, N.; Engelman,
A.; Xavier, R. J.; Lieberman, J.; Elledge, S. J.: Identification
of host proteins required for HIV infection through a functional genomic
screen. Science 319: 921-926, 2008.
2. Kataoka, N.; Bachorik, J. L.; Dreyfuss, G.: Transportin-SR, a
nuclear import receptor for SR proteins. J. Cell Biol. 145: 1145-1152,
1999.
3. Lai, M.-C.; Lin, R.-I.; Huang, S.-Y.; Tsai, C.-W.; Tarn, W.-Y.
: A human importin-beta family protein, transportin-SR2, interacts
with the phosphorylated RS domain of SR proteins. J. Biol. Chem. 275:
7950-7957, 2000.
*FIELD* CN
Paul J. Converse - updated: 2/29/2008
*FIELD* CD
Patricia A. Hartz: 4/7/2006
*FIELD* ED
alopez: 09/09/2011
mgross: 2/29/2008
mgross: 4/7/2006
*RECORD*
*FIELD* NO
610032
*FIELD* TI
*610032 TRANSPORTIN 3; TNPO3
;;TRANSPORTIN-SR; TRNSR
*FIELD* TX
DESCRIPTION
TNPO3 is a nuclear import receptor for serine/arginine-rich (SR)
read moreproteins, which are essential precursor-mRNA splicing factors (Kataoka
et al., 1999).
CLONING
Using the RS domain of ASF/SF2 (SFRS1; 600812) as bait in a yeast
2-hybrid screen, followed by screening a HeLa cell cDNA library, Kataoka
et al. (1999) cloned TNPO3, which they designated TRNSR. The deduced
975-amino acid protein has a calculated molecular mass of 109.8 kD. It
shows significant similarity to other importin-beta/transportin family
members (e.g., TNPO1; 602901), including a region required for RanGTP
(see RAN; 601179) binding.
By yeast 2-hybrid analysis using the RS domain of the E2 protein of
human papillomavirus (HPV)-5 as bait, Lai et al. (2000) cloned a TNPO3
splice variant, TRNSR2, from a HeLa cell cDNA library. The deduced
923-amino acid TRNSR2 protein lacks 2 regions of about 30 amino acids
each found in the TRNSR protein identified by Kataoka et al. (1999).
Northern blot analysis detected ubiquitous expression of a 4.5-kb
transcript, with highest expression in testis. Epitope-tagged TRNSR2
localized throughout transfected HeLa cells, but a mutant lacking the
N-terminal region colocalized with splicing factor SC35 (SFRS2; 600813)
in nuclear speckles.
GENE FUNCTION
Using in vitro binding assays, Kataoka et al. (1999) found that TRNSR
bound the RS domains of ASF/SF2 and SC35 directly, but it did not
interact with other protein domains examined. A Ran mutant mimicking
RanGTP, which promotes dissociation of import receptor-cargo complexes,
abolished binding of TRNSR to RS domains. In an in vitro import assay,
TRNSR efficiently imported the RS domains of ASF/SF2 and SC35 into the
nucleus in an ATP- and RanGDP-dependent manner. Far Western blot
analysis showed that TRNSR bound several proteins within an SR protein
fraction purified from HeLa nuclear extracts.
Using yeast 2-hybrid analysis, Lai et al. (2000) showed that TRNSR2
interacted with the RS domain in the hinge region of HPV-5 E2. The
C-terminal 400 amino acids of TRNSR2 also interacted with ASF/SF2, SC35,
and TRA2-beta (SFRS10; 602719). Mutation analysis confirmed that TRNSR2
interacted with the N-terminal RS domain of TRA2-beta, but not with the
RNA-binding domains of ASF and TRA2-beta. In vitro pull-down assays
revealed that only ASF containing phosphorylated RS domains interacted
with TRNSR2 in HeLa cell extracts. Lai et al. (2000) concluded that
TRNSR2 has a role in cellular trafficking of phosphorylated SR proteins.
Using a large-scale small interfering RNA screen to identify host
factors required by human immunodeficiency virus (HIV)-1 (see 609423),
Brass et al. (2008) identified more than 250 HIV-dependency factors
(HDFs), 79 of which showed significantly higher expression in immune
tissues compared with other tissues. Depletion of the HDF TNPO3, a
karyopherin, resulted in HIV inhibition after reverse transcription, but
before integration. Brass et al. (2008) proposed that targeting of HDFs
essential for the viral cycle but not critical for the host may avoid
drug resistance due to viral diversity and escape mutation.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the TNPO3
gene to chromosome 7 (TMAP D7S2931).
MOLECULAR GENETICS
- Association with Primary Biliary Cirrhosis
For a discussion of a possible association between variation in the
TNPO3 gene and primary biliary cirrhosis, see PBC4 (614220).
*FIELD* RF
1. Brass, A. L.; Dykxhoorn, D. M.; Benita, Y.; Yan, N.; Engelman,
A.; Xavier, R. J.; Lieberman, J.; Elledge, S. J.: Identification
of host proteins required for HIV infection through a functional genomic
screen. Science 319: 921-926, 2008.
2. Kataoka, N.; Bachorik, J. L.; Dreyfuss, G.: Transportin-SR, a
nuclear import receptor for SR proteins. J. Cell Biol. 145: 1145-1152,
1999.
3. Lai, M.-C.; Lin, R.-I.; Huang, S.-Y.; Tsai, C.-W.; Tarn, W.-Y.
: A human importin-beta family protein, transportin-SR2, interacts
with the phosphorylated RS domain of SR proteins. J. Biol. Chem. 275:
7950-7957, 2000.
*FIELD* CN
Paul J. Converse - updated: 2/29/2008
*FIELD* CD
Patricia A. Hartz: 4/7/2006
*FIELD* ED
alopez: 09/09/2011
mgross: 2/29/2008
mgross: 4/7/2006